ID A0A0D2K6E5_9EURO Unreviewed; 2381 AA.
AC A0A0D2K6E5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIY01393.1};
GN ORFNames=Z520_02945 {ECO:0000313|EMBL:KIY01393.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY01393.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY01393.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY01393.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN848065; KIY01393.1; -; Genomic_DNA.
DR RefSeq; XP_016635515.1; XM_016773458.1.
DR STRING; 1442371.A0A0D2K6E5; -.
DR GeneID; 27708691; -.
DR VEuPathDB; FungiDB:Z520_02945; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2299..2376
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2381 AA; 257086 MW; D9BF40FA0307F704 CRC64;
MPHASWTPGH DGSIAIVGLS CRFPGDASTP TKFWELLKNA KNAFTETTDR YNADAFYHPR
SGSVQNVIPT KGGYFLKEDL YEWDAAFFNI TAAEAMALDP RQRIAMEVTY EALENAGMPL
QKVSGSQTAC YMGSSMSDYR DSVSRDFQNY PKYHILGMSD EMIANRISHF LNIHGPSATV
QTACSSSLVS THIACQSLRS GESDMAIAGG VGLILGTEGT SHLNNLGFLN PAGHSRSFDA
DAGGYGRGEG CGVLILKRLE TAIQDGDNIR AVIRASGVNS DGWTPGVTMP SLLAQAALIK
KVYESSELDY GLTQYVEAHG TGTKAGDPIE TSAIHQTIGQ SKWRKKLYVG SVKPNIGHLE
AAAGVASIIK GVLALEHGMI PPNLNFTKPN PAIPLDEWNM VVPTRLTPWP AAQTKRMSIS
GFGMGGTNAH IVLDGYNLPA KTTNGVPASR KSASKRLFLL SSQDKAGFQR VGQSLSEYLG
NLGAAASSPA YLSNLAYTLA KARSGLAWRD AMIAENAAEL REHLTRSLGE GAVRAPNSAP
RIGFVFTGQG AQWARMGIEL MDRSVFSASI ARSAQYLRDL GCDWDPVNEL SAFEKDSRLG
VPLISQPICT VLQVALVDEL RSWGVTPSKV VGHSSGEIAA AYTLGALSHR DAVAAAYYRG
TVSSTPKLAA KNGGMMAVGC SPDEATALME ENNLSATVAC VNSPSSVTLS GDVKTLEAIK
AILNLRGTFA RRLKVGVAYH SSHMHSVSMD YYAAIAEVGQ DDILSDLQQQ RESVSMVSSV
SGHEVDASDL GPYYWVQNLI SPVLFADAVK ELVVPANSNG EKTVDLLIEV GPHSALGGPI
EQTLRSITGV HYTSMLVRNQ SALDTSMALA AELFRHGVSF DVAKVNADAN CKLLTDLPPY
AWNHSQKFSA IGRMQREQYT QQFPTRSLLG AMMPTMDERE RVWRSFIRLN DEPWLRGHMV
GSTVLFSAAG MVSIALEAAQ QVVEAHKTPL SFKLRDVSFV AAMALTEDMA TETVVHMRPH
LLATTGNPQS FWWEFSLSSC AGPAGQLREN CRGLISVIYG ESRSTYMAHE DAQTEAIRIA
DYRAVLKELP ENYSKESFYN IFAKSGFPYG EIFQGVETCH PGVGKTCYEV KVVDIGETFT
RGKLERPFLI HAATLDSMWQ GWLGSTQDYA APGDLGTEKP LVPTSIGELE VSMAMPGDIG
YSIPGICRSR RRGFDEFSAN ISMFDKDLSK VVVSVSNLHL SPLETESGAE AGAAAVVDPA
EIASEVRWNY PLDAMVPEEI EQALLSTDSA TPNARLLQLI QMVIHQHPAA KVIELVHSSK
DLPYTAMSKL LEGVIHHTQV QYAVAEGEGS ISDEVFGQPF ALGPLDAPLP SDITPADLFV
VPYDLSLKFK RNLNSYVERL VRMAKPGAMI AIAIPAAVPA QDTKSLNLKA NGFDLVSSTQ
ANGEILTFYK QAGEKQINSL LANGTHQEDE VVILPAESSK GSQSFANKLQ DMLHVQGYGV
TIEKGTPEIE SGDEKSYICL LELEKPFLEN LTEADFLGIR KLMLRARRLL WVTCGDSPSL
NMVDGLARCV NTEAAASNFQ VLHLSRQGEK SGPSLVTRIL TSSNQSADKE FREVGGLLQV
PRVYEAPEEN QQIRNHLQDS VQNISLSDDS AAFRLVIGKP GLLGSLNFVR DESLLAEPLG
DDELELDVKA AGVNFRDIMA CMGLVAVPGL GVEASGVVLK AGKNASKTFQ PGDRVSTLSL
GGAHATRTRC DYRVTAAVPD TMSFEEAAGA PTAHATAYFA LVRLARCREG QSVLIHAATG
GVGQAAIQLA RHLGLIIYAT VGTDDKRQLL KEQYGIPDEH IFHSRDSSFA KGVQRVTGGR
GVDCVLNSLS GELLRVSWTC LAPFGTFVEI GTRDITDNMR LDMRPFAKLA TFTSFDIATT
IEEDPAALGE ALQSAFQLLR QGKLHVPKPL TVYPCGQAES VFRTVQQGKH RGKFVLSFSG
ESKMKAPVMC KAKDSLRLDP GVTYLIVGGL GGLGRSLAKE FVASGARHIA FLSRSGDSKP
EAKATVDQLE QLGASVKVLR GDVADQTAFH RAMAECAQEF PPIKGVIQMA MVLRDTLIEN
MSYEDWKIPV EPKVRGTWNL HQYFNHERPL DFMIFCSSFT GIVGNAGQAQ YVAGNTYQDA
LAIYRRAHGL KAVSIDLGVM MEVGVIQEGA GHNFKQWEEV LGIRESTFSA LMKSLINGQQ
NRRSTERECP PHLTVGLGTG DIIAAHGLPP PRWFQDVRFG PLAVVSNLSS PTSGGEDKGA
GAPLATQLAA AAQDKDFAAA ATIITGALAA KLAEILRIPL SEIDSSRPLY SYGVDSLVAL
EVRNWITREI KANTALLDIL AAVPIETFAS QIAQKSKLVV G
//
